Novel hepatoprotective peptides derived from protein hydrolysates of mealworm (Tenebrio molitor).

In the present study, we hypothesized that protein hydrolysates of mealworm (Tenebrio molitor) which is known to exert significant scavenging activity toward reactive oxygen species (ROS) might protect liver cells against ROS-induced cytotoxicity. Therefore, hepatoprotective effects of protein hydrolysates of mealworm and their underlying mechanisms were investigated in AML12 mouse liver cells and the responsible peptides were further identified. Pretreatment with the mealworm alcalase hydrolysate (MAH; <1 kDa) showed the highest protective effect against HO-induced cytotoxicity in AML12 cells among three mealworm hydrolysates produced by different proteases (alcalase, flavourzyme, and neutrase). Further mechanistic studies demonstrated that MAH reduces ROS levels through increasing NF-E2-related factor 2-mediated expression of catalase, heme oxygenase-1, and genes involved in glutathione synthesis. Moreover, two novel hepatoprotective peptides, Ala-Lys-Lys-His-Lys-Glu and Leu-Glu, which shared similar mechanisms of action with MAH were identified. These results suggest that MAH and the two peptides represent potential sources of natural hepatoprotective agents.